4L79

Crystal Structure of nucleotide-free Myosin 1b residues 1-728 with bound Calmodulin

4L79 の概要

• エントリーDOI: 10.2210/pdb4l79/pdb
• 分子名称: Unconventional myosin-Ib, Calmodulin, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: myosin motor, actin binding, nucleotide hydrolysis, cargo, membrane binding, ca2+ binding, motor protein-metal binding protein complex, motor protein/metal binding protein
• 由来する生物種: Rattus norvegicus (brown rat,rat,rats); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton, spindle: P62158
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 102878.86

構造登録者

Shuman, H.,Zwolak, A.,Dominguez, R.,Ostap, E.M. (登録日: 2013-06-13, 公開日: 2014-01-29, 最終更新日: 2023-09-20)

主引用文献

Shuman, H.,Greenberg, M.J.,Zwolak, A.,Lin, T.,Sindelar, C.V.,Dominguez, R.,Ostap, E.M.
A vertebrate myosin-I structure reveals unique insights into myosin mechanochemical tuning.
Proc.Natl.Acad.Sci.USA, 111:2116-2121, 2014

PubMed Abstract: Myosins are molecular motors that power diverse cellular processes, such as rapid organelle transport, muscle contraction, and tension-sensitive anchoring. The structural adaptations in the motor that allow for this functional diversity are not known, due, in part, to the lack of high-resolution structures of highly tension-sensitive myosins. We determined a 2.3-Å resolution structure of apo-myosin-Ib (Myo1b), which is the most tension-sensitive myosin characterized. We identified a striking unique orientation of structural elements that position the motor's lever arm. This orientation results in a cavity between the motor and lever arm that holds a 10-residue stretch of N-terminal amino acids, a region that is divergent among myosins. Single-molecule and biochemical analyses show that the N terminus plays an important role in stabilizing the post power-stroke conformation of Myo1b and in tuning the rate of the force-sensitive transition. We propose that this region plays a general role in tuning the mechanochemical properties of myosins.

PubMed: 24469830
DOI: 10.1073/pnas.1321022111

実験手法

X-RAY DIFFRACTION (2.3 Å)